PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
15901356-7	2005	beta-glucosidase or beta-galactosidase (lactase/phloridzin hydrolase, LPH) and alpha-glucosidase (sucrase-isomaltase) had different pH-dependent activities for disaccharide conjugates.	Disaccharides	160-172	galactosidase beta 1	Homo sapiens	20-38	
15703907-2	2005	The beta-galactosidase activity of whole bifidobacterial cells showed an optimum activity at pH 6.8-7.0 and 40 degrees C. The transgalactosylation activity of the B. bifidum cells from 50% (w/w) lactose resulted in a galactooligosaccharide mixture (20% w/w) comprising (w/w): 25% disaccharides, 35% trisaccharides, 25% tetrasaccharides and 15% pentasaccharides.	Disaccharides	280-293	galactosidase beta 1	Homo sapiens	4-22	
15034616-1	2004	In examining C-6 modified 4-nitrophenyl beta-D-galactopyranosides as donor structures the beta-galactosidase (Bacillus circulans) revealed an unexpectedly broad substrate specificity which allowed successful syntheses of various disaccharide components.	Disaccharides	229-241	galactosidase beta 1	Homo sapiens	90-108	
20967490-0	2011	The use of disaccharides in inhibiting enzymatic activity loss and secondary structure changes in freeze-dried beta-galactosidase during storage.	Disaccharides	11-24	galactosidase beta 1	Homo sapiens	111-129	
3119960-0	1987	Disaccharide synthesis with immobilized beta-galactosidase.	Disaccharides	0-12	galactosidase beta 1	Homo sapiens	40-58	
4026310-7	1985	Digestion with neuraminidase and beta-galactosidase of the O-linked oligosaccharides supported the idea that the common disaccharide core was mainly of the structure beta-galactosyl-N-acetylgalactosamine.	Disaccharides	120-132	galactosidase beta 1	Homo sapiens	33-51	
34223948-1	2021	The enzyme beta-galactosidase has great potential for application in the food and pharmaceutical industries due to its ability to perform the hydrolysis of lactose, a disaccharide present in milk and in dairy by-products.	Disaccharides	167-179	galactosidase beta 1	Homo sapiens	11-29	
20967490-1	2011	PURPOSE: The purpose of this study is to show how disaccharides differ in their ability to protect lyophilized beta-galactosidase from enzymatic activity loss and secondary structure changes during storage.	Disaccharides	50-63	galactosidase beta 1	Homo sapiens	111-129	
19966440-8	2009	Structural comparisons of (II) with related disaccharides bound to a mutant beta-galactosidase reveal significant differences in hydroxymethyl conformation and in the degree of ring distortion of the betaGlcp residue.	Disaccharides	44-57	galactosidase beta 1	Homo sapiens	76-94